Spectral studies on the calcium‐binding properties of Mts1 protein and its interaction with target protein

FEBS Letters

Lomonosov, M.Y³  Lukanidin, E.M³  Dukhanina, E.A¹  Georgiev, G.P¹  Dukhanin, A.S² 

[1] Engelhardt Institute of Molecular Biology, Russian Academy of Science, Vavilov Str. 32, Moscow 117984, Russian Federation;Russian State Medical University, Ostrovityanova Str. 1, Moscow 117457, Russian Federation;Institute of Gene Biology, Russian Academy of Science, Vavilov Str. 34/5, Moscow 117334, Russian Federation

关键词: S-100 protein;    Calcium;    Mts1;    Fluo-3;    Target protein;   

DOI  :  10.1016/S0014-5793(97)00576-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two calcium-binding sites of the Mts1 protein, a member of S-100 protein family, were distinguished with the Fluo-3 fluorescent technique. The geometric mean of the apparent dissociation constant () for these two sites is 2.6 μM; the Hill coefficient (n _H) is 0.98. In the presence of a novel target protein p37, isolated from the mouse adenocarcinoma cell line CSML-100, Mts1 binds Ca²⁺ ions with higher affinity and with strong positive cooperativity (=0.2 μM, n _H=1.91). Interaction of Mts1 with p37 is confirmed by the fluorescent probe 2-p-toluidinylnaphthalene-6-sulfonate (TNS). Reaction with TNS shows that p37 interacts with the hydrophobic site of Mts1 which is exposed due to the binding of Ca²⁺ ions.

【 授权许可】

Unknown